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Biochem Soc Trans ; 32(Pt 6): 943-5, 2004 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-15506931

RESUMO

FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl beta-hydroxylase belonging to the super-family of 2-oxoglutarate and Fe(II)-dependent dioxygenases, catalyses hydroxylation of Asn-803 of hypoxia-inducible factor, a transcription factor that regulates the mammalian hypoxic response. Only one other asparaginyl beta-hydroxylase, which catalyses hydroxylation of both aspartyl and asparaginyl residues in EGF (epidermal growth factor)-like domains, has been characterized. In the light of recent crystal structures of FIH, we compare FIH with the EGFH (EGF beta-hydroxylase) and putative asparagine/asparaginyl hydroxylases. Sequence analyses imply that EGFH does not contain the HXD/E iron-binding motif characteristic of most of the 2-oxoglutarate oxygenases.


Assuntos
Oxigenases de Função Mista/metabolismo , Proteínas Repressoras/metabolismo , Sequência de Aminoácidos , Asparagina/metabolismo , Sítios de Ligação , Ferro/metabolismo , Dados de Sequência Molecular , Pró-Colágeno-Prolina Dioxigenase/metabolismo , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos
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